Parsonage D - Search Results

1

Equilibrium analyses of the active-site asymmetry in enterococcal NADH oxidase: role of the cysteine-sulfenic acid redox center.

Mallett TC, Parsonage D, Claiborne A. Mallett TC, et al. Among authors: parsonage d. Biochemistry. 1999 Mar 9;38(10):3000-11. doi: 10.1021/bi9817717. Biochemistry. 1999. PMID: 10074352

2

Structure of the type III pantothenate kinase from Bacillus anthracis at 2.0 A resolution: implications for coenzyme A-dependent redox biology.

Nicely NI, Parsonage D, Paige C, Newton GL, Fahey RC, Leonardi R, Jackowski S, Mallett TC, Claiborne A. Nicely NI, et al. Among authors: parsonage d. Biochemistry. 2007 Mar 20;46(11):3234-45. doi: 10.1021/bi062299p. Epub 2007 Feb 27. Biochemistry. 2007. PMID: 17323930 Free PMC article.

3

Structure of alpha-glycerophosphate oxidase from Streptococcus sp.: a template for the mitochondrial alpha-glycerophosphate dehydrogenase.

Colussi T, Parsonage D, Boles W, Matsuoka T, Mallett TC, Karplus PA, Claiborne A. Colussi T, et al. Among authors: parsonage d. Biochemistry. 2008 Jan 22;47(3):965-77. doi: 10.1021/bi701685u. Epub 2007 Dec 23. Biochemistry. 2008. PMID: 18154320

4

Crystal structure and catalytic properties of Bacillus anthracis CoADR-RHD: implications for flavin-linked sulfur trafficking.

Wallen JR, Mallett TC, Boles W, Parsonage D, Furdui CM, Karplus PA, Claiborne A. Wallen JR, et al. Among authors: parsonage d. Biochemistry. 2009 Oct 13;48(40):9650-67. doi: 10.1021/bi900887k. Biochemistry. 2009. PMID: 19725515 Free PMC article.

5

Structural Analysis of Streptococcus pyogenes NADH Oxidase: Conformational Dynamics Involved in Formation of the C(4a)-Peroxyflavin Intermediate.

Wallen JR, Mallett TC, Okuno T, Parsonage D, Sakai H, Tsukihara T, Claiborne A. Wallen JR, et al. Among authors: parsonage d. Biochemistry. 2015 Nov 17;54(45):6815-29. doi: 10.1021/acs.biochem.5b00676. Epub 2015 Nov 6. Biochemistry. 2015. PMID: 26506002

6

Analysis of the kinetic mechanism of enterococcal NADH peroxidase reveals catalytic roles for NADH complexes with both oxidized and two-electron-reduced enzyme forms.

Crane EJ 3rd, Parsonage D, Poole LB, Claiborne A. Crane EJ 3rd, et al. Among authors: parsonage d. Biochemistry. 1995 Oct 31;34(43):14114-24. doi: 10.1021/bi00043a016. Biochemistry. 1995. PMID: 7578008

The combined rapid-reaction and steady-state data are best accommodated by a limiting type of ternary complex mechanism very similar to that proposed previously [Parsonage, D., Miller, H., Ross, R.P., & Claiborne, A. (1993) J. Biol. Chem. 268, 3161-3167]....

The combined rapid-reaction and steady-state data are best accommodated by a limiting type of ternary complex mechanism very similar to that …

7

An L40C mutation converts the cysteine-sulfenic acid redox center in enterococcal NADH peroxidase to a disulfide.

Miller H, Mande SS, Parsonage D, Sarfaty SH, Hol WG, Claiborne A. Miller H, et al. Among authors: parsonage d. Biochemistry. 1995 Apr 18;34(15):5180-90. doi: 10.1021/bi00015a032. Biochemistry. 1995. PMID: 7711038

8

Crystallographic analyses of NADH peroxidase Cys42Ala and Cys42Ser mutants: active site structures, mechanistic implications, and an unusual environment of Arg 303.

Mande SS, Parsonage D, Claiborne A, Hol WG. Mande SS, et al. Among authors: parsonage d. Biochemistry. 1995 May 30;34(21):6985-92. doi: 10.1021/bi00021a010. Biochemistry. 1995. PMID: 7766608

9

Analysis of the kinetic and redox properties of NADH peroxidase C42S and C42A mutants lacking the cysteine-sulfenic acid redox center.

Parsonage D, Claiborne A. Parsonage D, et al. Biochemistry. 1995 Jan 17;34(2):435-41. doi: 10.1021/bi00002a007. Biochemistry. 1995. PMID: 7819235

10

Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation.

Claiborne A, Miller H, Parsonage D, Ross RP. Claiborne A, et al. Among authors: parsonage d. FASEB J. 1993 Dec;7(15):1483-90. doi: 10.1096/fasebj.7.15.8262333. FASEB J. 1993. PMID: 8262333 Review.

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